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Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention
Open accessAbstract
There is considerable interest in the role that mammalian heme peroxidase enzymes, primarily myeloperoxidase, eosinophil peroxidase and lactoperoxidase, may play in a wide range of human pathologies. This has been sparked by rapid developments in our understanding of the basic biochemistry of these enzymes, a greater understanding of the basic chemistry and biochemistry of the oxidants formed by these species, the development of biomarkers that can be used damage induced by these oxidants in vivo, and the recent identification of a number of compounds that show promise as inhibitors of these enzymes. Such compounds offer the possibility of modulating damage in a number of human pathologies. This reviews recent developments in our understanding of the biochemistry of myeloperoxidase, the oxidants that this enzyme generates, and the use of inhibitors to inhibit such damage.
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“The reaction catalyzed by MPO is the oxidation of the Cl− anion by H2O2 to give hypochlorous acid HOCl, a very reactive and oxidizing agent, which can also act as a chlorinating agent and is the main strong oxidant generated by neutrophils in appreciable quantities [30].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [30]
In the citing paper
“The reaction catalyzed by MPO is the oxidation of the Cl− anion by H2O2 to give hypochlorous acid HOCl, a very reactive and oxidizing agent, which can also act as a chlorinating agent and is the main strong oxidant generated by neutrophils in appreciable quantities [30].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [30]
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“Hypochlorous acid HOCl and hypothiocyanous acid HOSCN synthesized through the enzyme myeloperoxidase MPO, which catalyzes the reaction between H2O2 and Cl− or SCN−, are important inorganic bactericidal molecules, effective against a wide range of microbes.”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [30]
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Citations
Cites
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455
Dietary phenolics: chemistry, bioavailability and effects on health
Crozier, A., Jaganath, I. B., & Clifford, M. N. (2009) · Natural Product Reports · doi:10.1039/b802662a · Cited by 2,062
Nitric oxide, oxidants, and protein tyrosine nitration
Radí, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307446101 · Cited by 1,477
The oxidative environment and protein damage
Davies, M. J. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.08.007 · Cited by 1,392
Self-citationDaugherty, A., Dunn, J. L., Rateri, D. L., & Heinecke, J. W. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117342 · Cited by 1,269
Phagocytes and oxidative stress
Babior, B. M. (2000) · The American Journal of Medicine · doi:10.1016/s0002-9343(00)00481-2 · Cited by 1,061
The Acid Ionization Constant of HOCl from 5 to 35°
Morris, J. C. (1966) · The Journal of Physical Chemistry · doi:10.1021/j100884a007 · Cited by 927
Myeloperoxidase-Halide-Hydrogen Peroxide Antibacterial System
Klebanoff, S. J. (1968) · Journal of Bacteriology · doi:10.1128/jb.95.6.2131-2138.1968 · Cited by 820
Pattison, D. I., & Davies, M. J. (2001) · Chemical Research in Toxicology · doi:10.1021/tx0155451 · Cited by 790
Self-citationZheng, L., Nukuna, B. N., Brennan, M., Sun, M., Goormastic, M., Settle, M., Schmitt, D., Fu, X., Thomson, L., Fox, P. L., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21109 · Cited by 735
Research works printed but not linked: 2
- 174 <citation><person-group person-group-type = "editor"><name><surname>Lentner</surname><given-names>C</given-names></name></person-group><source>Geigy Scientific Tables vol. 3: Physical Chemistry, Composition of Blood, Hematology, Somatometric Data</source>Basle, Ciba-Geigy Ltd, <year>1984</year></citation>
- 226 Kettle AJ, Gedye CA, Winterbourn CC. Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic acid hydrazide. Biochem J 1997; 321: 503-508. · DOI
Cited by
Sorted by citations
Items 301–400 of 416
Kumar, G., Saini, M., & Kundu, S. (2021) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2020-0732 · Cited by 6
Markers involved in proinflammatory effects by environmental toxicants
Smiljevska-Ristovska, V., Sabriu-Haxhijaha, A., Ristoski, T., Kosharkoska‐Spasovska, F., Krstanoski, L., & Dimitrova‐Shumkovska, J. (2020) · Toxicology Mechanisms and Methods · doi:10.1080/15376516.2020.1791293 · Cited by 6
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Sengupta, P., Dutta, S., Henkel, R., Rosas, I. M., & Roychoudhury, S. (2026) · Frontiers in Endocrinology · doi:10.3389/fendo.2026.1747453 · Cited by 5
Fu, Y., Wang, H., Liu, Z., Zhang, F., Wang, H., Wu, Z., Shen, Q., & Guo, S. (2024) · Future Foods · doi:10.1016/j.fufo.2024.100352 · Cited by 5
Ramírez, D. C., & Gomez-Mejiba, S. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8098 · Cited by 7
Nandeshwar, R., Illa, M. P., Khandelwal, M., & Tallur, S. G. (2022) · Biosensors and Bioelectronics X · doi:10.1016/j.biosx.2022.100252 · Cited by 5
Pirogov, A. B., Prikhodko, A. G., Zinovev, S., Borodin, E. A., Ushakova, E. V., Makarova, G. A., & Perelman, J. M. (2017) · Bulletin of Siberian Medicine · doi:10.20538/1682-0363-2017-2-159-169 · Cited by 5
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Xiao, R., & He, R. (2017) · Springer eBooks · doi:10.1007/978-94-024-1177-5_2 · Cited by 5
Kostevich, V. A., & Av, S. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.08.003 · Cited by 5
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Siddiquee, K., Zhao, C., Stemler, M., Zeck, B., Fishpaugh, J. R., & Allen, S. P. (2019) · Bioresources and Bioprocessing · doi:10.1186/s40643-019-0270-8 · Cited by 5
Ferdous, M., Sonam Chhoden, R., Mudi, S. R., Ali, M., Jasmin, S., Fariduddin, M., Alam, S. M. K., Arslan, M., & Biswas, S. K. (2020) · Diabetes & Metabolic Syndrome Clinical Research & Reviews · doi:10.1016/j.dsx.2020.01.001 · Cited by 6
Rabha, M., Sheet, S. K., Sen, B., Konthoujam, I., Aguan, K., & Khatua, S. (2023) · ChemistrySelect · doi:10.1002/slct.202204643 · Cited by 5
Clemen, R., Fuentes-Lemus, E., Bekeschus, S., & Davies, M. J. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102835 · Cited by 6
Self-citationBehera, A., Mane, S., Hemadri, V. A., Bhand, S., & Tripathi, S. (2023) · IEEE Sensors Letters · doi:10.1109/lsens.2023.3330095 · Cited by 5
Magaji, U. F., Köroğlu, P., Cöremen, M., Bulan, Ö. K., Saçan, Ö., & Yanardağ, R. (2024) · Journal of Molecular Histology · doi:10.1007/s10735-024-10345-8 · Cited by 4
Akinrinde, A. S., Fapuro, J., & Soetan, K. O. (2021) · Beni-Suef University Journal of Basic and Applied Sciences · doi:10.1186/s43088-021-00108-9 · Cited by 4
Stambekova, D., & O’Reilly, R. J. (2017) · Chemical Data Collections · doi:10.1016/j.cdc.2017.07.002 · Cited by 4
Advanced Oxidation Protein Product (AOPP) Levels in Second- and Third-Degree Thermal Burns
Mert, H., Açıkkol, S., Çallı, İ., ÇİBUK, S., Keskin, S., & Mert, N. (2020) · Journal of Burn Care & Research · doi:10.1093/jbcr/iraa127 · Cited by 4
Electrochemical quantification of biomarker myeloperoxidase
Hoyo, J., Bassegoda, A., & Tzanov, T. (2022) · Zeitschrift für Naturforschung C · doi:10.1515/znc-2021-0274 · Cited by 4
Kariyawasam, V. C., Davis, T., Ghali, M., Tejcek, D., O’Neil, T. R., Verley, E., Griffiths, M., Campos, M. A. L., Bonney, I., Bulmer, A. C., et al. (2025) · Advanced Healthcare Materials · doi:10.1002/adhm.202501825 · Cited by 3
Balkrishna, A., Sinha, S., Manik, M., Pandey, A., Maity, M., Dev, R., & Varshney, A. (2024) · Discovery Medicine · doi:10.24976/discov.med.202436183.75 · Cited by 3
Lin, X., Dong, Q., Chang, Y.-L., Zhang, S., & Shi, P. (2024) · Chemosensors · doi:10.3390/chemosensors12080166 · Cited by 3
Antelmann, H. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-818619-0.00051-4 · Cited by 4
Nijakowski, K., Rutkowski, R., Gruszczyński, D., Witowski, J., Surdacka, A., & Kanikowska, D. (2024) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2901010 · Cited by 3
Khare, S. P., Deshmukh, T. R., Sangshetti, J. N., Khedkar, V. M., & Shingate, B. B. (2024) · Polycyclic aromatic compounds · doi:10.1080/10406638.2024.2309358 · Cited by 3
Magaji, U. F., Cöremen, M., Bulan, Ö. K., Saçan, Ö., & Yanardağ, R. (2024) · Journal of Medicinal Food · doi:10.1089/jmf.2023.0091 · Cited by 3
Sukhishvili, N., Franck, T. J., Mouithys-Mickalad, A., Frédérich, M., Mulkijanyan, K., Sandersen, C., Serteyn, D. A., & Mskhiladze, L. (2024) · The Natural Products Journal · doi:10.2174/0122103155334830240912072007 · Cited by 3
Pro-inflammatory Markers of Environmental Toxicants
Dimitrova‐Shumkovska, J., Veenman, L., & Krstanoski, L. (2023) · Biomarkers in disease · doi:10.1007/978-3-031-07392-2_11 · Cited by 3
Investigation of oxidative metabolism of uric acid and its role in redox processes in inflammation
da Silva, R. P. (2020) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.46.2020.tde-29092021-142945 · Cited by 3
Kouki, A., Marrouchi, R., Souli, A., Bouabdallah, S., Ferjani, W., Dang, P. M., Dıcko, A., Benna, J. E., & Ben‐Attia, M. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01998-2 · Cited by 2
Update on antineutrophil cytoplasmic antibody vasculitis
Mandel, D. A., Shekhar, N., Hanna, R. M., & Reddy, U. G. (2025) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0000000000001146 · Cited by 2
Myeloperoxidase in the pathogenesis of sickle cell disease
Biernat, M. M., Camp, O. G., Awonuga, A. O., Abu‐Soud, H. M., Chatzicharalampous, C., Kofinas, G., & Kofinas, J. D. (2026) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2026.110800 · Cited by 2
Implications of bacterial exposure to reactive oxygen and chlorine species
Donkor, G. Y., & Dahl, J. (2026) · Infection and Immunity · doi:10.1128/iai.00010-23 · Cited by 2
Kocamaz, H., Özdemir, Ö. M. A., Türk, N. Ş., Enli, Y., Şahin, B., & Ergin, H. (2020) · Bosnian Journal of Basic Medical Sciences · doi:10.17305/bjbms.2020.4823 · Cited by 2
Yoon, Y., Kim, H., & Lee, J. (2021) · Oral Biology Research · doi:10.21851/obr.45.03.202109.99 · Cited by 2
(2022) · Biointerface Research in Applied Chemistry · doi:10.33263/briac132.198 · Cited by 2
Zhang, F., Mo, Y., Cao, X., Zhou, Y., Liu, Y. D., & Zhong, R. (2024) · Organic & Biomolecular Chemistry · doi:10.1039/d3ob02111d · Cited by 2
Antioxidant Therapy in CVD: Hope or Hype
Nasser, S. A., & Dent, G. (2024) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-3-031-62131-4_6 · Cited by 2
Pinto, L. D. S., Alves, R. S., Lopes, B. R. P., da Silva, G. S., Menezes, G. D. L., Moreira, P. A. M., de Oliveira, J., da Silva, R. A., Lousa, D., & Toledo, K. A. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.137423 · Cited by 2
Souza, R., da Costa, A., & Oliveira, B. (2022) · Asian journal of Current Research in Clinical Cancer · doi:10.51847/rwvdkpqcqr · Cited by 2
Aissat, S., Benbarek, H., Franck, T. J., Kohnen, S. L., Deby-Dupont, G. P., Serteyn, D. A., Ahmed, M., & Mouithys-Mickalad, A. A. (2015) · Frontiers in Life Science · doi:10.1080/21553769.2015.1044131 · Cited by 2
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Yunanto, A., Hartoyo, E., Thalib, I., Putri, N. A., & Suhartono, E. (2021) · International Journal of Applied Pharmaceutics · doi:10.22159/ijap.2021.v13s1.y0072 · Cited by 2
Suga, N., Murakami, A., Arimitsu, H., Shiogama, K., Tanaka, S., Ito, M., & Kato, Y. (2021) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.20-161 · Cited by 2
Mechanism of peroxidasin inactivation in hyperglycemia: Heme damage by reactive oxygen species
Ivanov, S. V., Rose, K. L., Colon, S., Hudson, B. G., Bhave, G. B., & Voziyan, P. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.149237 · Cited by 2
ASSESSMENT OF OXIDATIVE STRESS AND ANTIOXIDANT STATUS IN TYPE 1 DIABETES MELLITUS
Fathi, F. H., Mohammad, J. A., & Almulathanon, A. A. Y. (2023) · Military Medical Science Letters · doi:10.31482/mmsl.2023.015 · Cited by 1
Epigenetic integration of signaling from the regenerative environment
Geara, P., & Dilworth, F. J. (2024) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2024.02.003 · Cited by 1
Therapeutic Use of Carbon Monoxide in Ex-Vivo Lung Perfusion in Donor With Prolonged Cold Ischemia
Mussi, R. K., Nakajima, D., Chen, M., Maahs, L., Coutinho, R., Qaqish, R. T., Liu, M., Keshavjee, S. H., & Cypel, M. (2024) · Journal of Surgical Research · doi:10.1016/j.jss.2024.05.048 · Cited by 3
Role of Nitric oxide synthase II in cognitive impairment due to experimental cerebral malaria
Igreja-Silva, T., Cunha‐Fernandes, T., Moreira, E. T. D. S., Ferreira, A. D. C., Estato, V., Castro-Faria-Neto, H. C., & dos Reis, P. R. P. (2024) · Nitric Oxide · doi:10.1016/j.niox.2024.10.002 · Cited by 1
Wang, T., Yang, J., Yang, T., Zhou, F., Tu, S., Yan, L., Le, Y., & Liu, L. (2025) · Dyes and Pigments · doi:10.1016/j.dyepig.2025.113441 · Cited by 1
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Patrão-Neto, F. C., Tomaz, M. A., & Melo, P. A. (2017) · Toxinology · doi:10.1007/978-94-007-6452-1_9 · Cited by 1
Helal, B. A. E., Elshrbiny, R. A., & Shebl, M. M. (2017) · The Egyptian Journal of Hospital Medicine · doi:10.12816/0040628 · Cited by 1
Zhang, H., Lan, P., Yang, Q., Li, C., Zhao, L., Kang, X., & Li, Y. (2023) · Canadian Journal of Chemistry · doi:10.1139/cjc-2023-0009 · Cited by 1
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Grigorieva, D. V., Gorudko, I. V., Reut, V. E., Simakin, A. V., Kostevich, V. A., Gorbunov, N., Panasenko, O. M., & Sokolovc, A. V. (2024) · Journal of Applied Spectroscopy · doi:10.1007/s10812-024-01723-x · Cited by 1
Enzymatic Degradation of Carbon Nanotubes and Mechanical Separation of Carbon Nanocups
Gaugler, J. A. (2016) · D-Scholarship@Pitt (University of Pittsburgh) · Cited by 1
Signaling by CO: Molecular and Cellular Functions
Foresti, R., Braud, L., & Motterlini, R. (2018) · Royal Society of Chemistry eBooks · doi:10.1039/9781788013000-00161 · Cited by 1
Malisorn, N., & Chaikan, A. (2021) · Tropical Journal of Pharmaceutical Research · doi:10.4314/tjpr.v18i9.3 · Cited by 1
Properties and functions of myeloperoxidase and its role in ovarian cancer
Gąsowska-Bajger, B., Gąsowska-Bodnar, A., & Bodnar, L. (2022) · MEDICAL SCIENCE PULSE · doi:10.5604/01.3001.0015.9645 · Cited by 1
THE NOVEL PHARMACOLOGICAL ACTIONS OF ISONIAZID: A PROPOSAL FOR ITS MODE OF ACTION
Khan, M. S. R. (2017) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3pc2tn21 · Cited by 1
Cayuela, N. C. (2018) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.5.2018.tde-11092018-152539 · Cited by 1
High Fructose Consumption: More Pain Than Gain to Human HealthPreprint
Isaiah, S., Olanrewaju, O. S., Sholeye, A. R., & Ayilara, M. S. (2021) · Preprints.org · doi:10.20944/preprints202106.0464.v1 · Cited by 1
Sultana, S., LeDoux, K., Crompton, M. E., Jankiewicz, O., Morales, G. H., Johnson, C., Horbach, E., Hoffmann, K. P., Kr, P., Shah, R., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.31.458474 · Cited by 1
Expression of Rcrb Confers Resistance to Hypochlorous Acid in Uropathogenic Escherichia Coli
Crompton, M. E. (2023) · ISU Red - Research and eData (Illinois State University) · doi:10.30707/etd2023.20230711063200956174.999989 · Cited by 1
Levitated Drop Microreactors for Biochemical Kinetics
Scheeline, A., Choi, W. H., Chainani, E. T., & Ngo, K. T. (2012) · Advanced materials research · doi:10.4028/www.scientific.net/amr.560-561.395
Biomarcadores relevantes para diagnóstico precoce e prevenção de doenças cardiovasculares.
Queiroz, J. C. S. (2014)
Sarkaratı, B. (2013) · Hacettepe University Institutional Repository (hacettepe.edu.tr)
Cristina, L., & Pereira, R. (2012)
Su, D. (2016) · University of Liverpool · doi:10.17638/02029279
Prashant, V. (2014) · International Journal of Pharma and Bio Sciences
Абатуров, А. Е., Volosovets, O. P., & Khudiakov, O. Y. (2016) · CHILD`S HEALTH · doi:10.22141/2224-0551.4.72.2016.76597
The Role Of Thiocyanate In Modulating Tissue Damage In Cardiovascular Disease
Hall, L. (2017) · The Sydney eScholarship Repository (The University of Sydney)
Baghdasarian, A. (2013) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r39s1kw71
Hanifeh, M. (2018) · Työväentutkimus Vuosikirja
Zanotto, C. Z. (2018) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.17.2018.tde-06042018-102417
Multifunctional enzymatically-generated hydrogel platforms for chronic wound application
Stefanov, I. (2019) · UPCommons institutional repository (Universitat Politècnica de Catalunya) · doi:10.5821/dissertation-2117-170447
[The role of neuroinflammation-related regulatory targets in the treatment for Parkinson’s disease].
Zang, C., Bao, X.-Q., Sun, H., & Zhang, D. (2016) · PubMed
Nedoboy, P. E. (2014) · UPT. Syiah Kuala University Library (Syiah Kuala University)
Coremans, C., Boudjeltia, K. Z., Antwerpen, P. V., & Delporte, C. (2021) · CRC Press eBooks · doi:10.1201/9781003212287-9
Biochemical Processes and Metal Complexes’ Role as Catalysts
Duca, G. G. (2012) · Springer series in chemical physics · doi:10.1007/978-3-642-24629-6_3
Sharma, V. K. (2012) · Wiley eBooks · doi:10.1002/9781118482469.ch3
Dexamethasone Antagonizes Myotoxic and Inflammatory Effects Induced by Bothrops Snake Venoms
Patrão-Neto, F. C., Tomaz, M. A., & Melo, P. A. (2015) · Springer eBooks · doi:10.1007/978-94-007-6726-3_9-1
Morrow, J. R. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.735332657.793567778
Pro-inflammatory Markers of Environmental Toxicants
Dimitrova‐Shumkovska, J., Veenman, L., & Krstanoski, L. (2022) · Biomarkers in disease · doi:10.1007/978-3-030-87225-0_11-1
Molecular and tissue basis of neuroinflammation in health and disease
(2023) · Advances in magnetic resonance technology and applications · doi:10.1016/b978-0-323-91771-1.00002-2
O’Reilly, R. J., & Karton, A. (2023) · Electronic Structure · doi:10.1088/2516-1075/acd234
Expression of RcrB confers resistance to hypochlorous acid in uropathogenic Escherichia coliPreprint
Crompton, M. E., Gaessler, L. F., Tawiah, P. O., Pfirsching, L., Camfield, S. K., Johnson, C., Meurer, K., Bennis, M., Roseberry, B., Sultana, S., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.01.543251
Aztatzi-Aguilar, O. G. (2022) · Biomedical Journal of Scientific & Technical Research · doi:10.26717/bjstr.2022.47.007444
Song, Y., & Wurtz, N. R. (2024) · Medicinal chemistry reviews · doi:10.1021/mc-2024-vol59.ch04
Puf, R., Smith, M. L., & Laaksonen, A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.27.645784
Pinheiro, L., Cipriano, C., Santos, F., Máximo, P., Fernandes, E. G. R., Freitas, M., & Branco, P. S. (2025) · Molecules · doi:10.3390/molecules30132850
Metabolism of Formaldehyde In Vivo
Xiao, R., & He, R. (2025) · Springer eBooks · doi:10.1007/978-981-96-7281-3_2
Biochemistry of free radicals and reactive oxygen species
Goswami, S. K. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-22335-8.00008-5
Musiał, N., Iwaniec, M. O., Mruk, I., Puchalski, M., Tretiakow, D., Skorek, A., Szydłowski, K., Szlęzak, J., & Czaplewska, P. (2026) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2026.1769952
Demonstration of extracellular traps in tuberculous pleural effusion from adult patients
Lal, G., Dass, M., Jindal, N., Singhal, R., Bhalla, M., Aggarwal, A. N., & Haldar, S. (2026) · Tuberculosis · doi:10.1016/j.tube.2026.102763
Dai, M., Ding, S., Wu, Z., Lu, H., Peng, S., Wang, S. Y., Wang, X., Liu, X., Li, F., Wei, P., et al. (2026) · Dyes and Pigments · doi:10.1016/j.dyepig.2026.113853
Hemin Recapitulates the Labile Iron Pool in the Cellular Fenton Reaction with DNA
Fleming, A. M., & Burrows, C. J. (2026) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.6c00203
Metadata
- Authors
- Davies, M. J.
- Affiliations
- The University of Sydney (AU)
- Corresponding author
- Davies, Michael J.
- ORCID
- Davies, Michael J.
- Venue
- Journal of Clinical Biochemistry and Nutrition
- Published
- 2010
- Volume
- 48
- Issue
- 1
- Pages
- 8-19
- ISSN
- 0912-0009 (ISSN-L)
- 1880-5086
- PMC
- PMC3022070
- OpenAlex
- W2028031080
- Cited by
- 412
- References
- 227
- Citations by year
- 2026: 18 · 2025: 15 · 2024: 31 · 2023: 30 · 2022: 34 · 2021: 40 · 2020: 41 · 2019: 37 · 2018: 27 · 2017: 29 · 2016: 23 · 2015: 21 · 2014: 19 · 2013: 16 · 2012: 24
- FWCI
- 6.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Biochemistry and Nutrition (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Fondation pour la Recherche Médicale
- Medical Research Council
- Australian Research Council (CE0561607, DP0988311)
- National Health and Medical Research Council (570829)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- myeloperoxidase, heme peroxidase, eosinophil peroxidase, lactoperoxidase, oxidative damage, oxidative damage biomarkers, enzyme inhibitors
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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